Laminin Pentapeptide YIGSR-NH₂ (Highly Pure) – Research Use Only

Laminin Pentapeptide YIGSR-NH₂ (Highly Pure) is a biotechnology-grade laminin-derived synthetic peptide supplied for research applications involving cell adhesion studies, extracellular matrix biology, biomaterials development, and receptor-mediated signaling workflows. This five-amino-acid sequence, derived from the laminin B1 chain, is widely used in experimental systems to investigate cell–matrix interactions, substrate functionalization, tissue engineering environments, and peptide-mediated biological responses. Its defined composition and compact sequence make it especially useful in cell culture, surface coating, hydrogel, and mechanistic in vitro assay development.

Scientific Overview

YIGSR is a well-characterized laminin-derived pentapeptide that has been widely studied for its role in cell adhesion and extracellular matrix-related biological interactions. As a short bioactive motif from the laminin B1 chain, it is frequently used in experimental systems where researchers want to isolate or reproduce specific matrix-derived signaling effects in a more controlled format than full-length ECM proteins.

In research workflows, YIGSR-NH₂ is commonly applied in surface functionalization, biomaterial design, scaffold engineering, peptide–receptor studies, and cell behavior assays. Because of its small size and defined sequence, it is especially useful in studies involving cell attachment, migration, substrate response, neural and epithelial model systems, and tumor-related mechanistic investigations.

Applications

• Cell adhesion and extracellular matrix interaction studies
• Biomaterial, scaffold, and hydrogel functionalization
• Cell culture substrate coating and attachment workflows
• Peptide–receptor and matrix signaling investigations
• Tissue engineering, cancer biology, and regenerative research models

Usage & Handling Guidance

Store at −20°C as specified. Reconstitution should be performed using an appropriate solvent or buffer depending on the intended application, coating protocol, or material system. Researchers should optimize concentration, immobilization conditions, and exposure parameters according to the cell type or assay platform being used.

• Preparation: Reconstitute in a suitable solvent or buffer for the intended workflow
• Handling: Use standard peptide handling practices and avoid repeated unnecessary freeze–thaw cycles
• Optimization: Adjust concentration based on coating density, matrix composition, or cell response requirements
• Workflow note: Validate performance in the intended in vitro or biomaterials system

What You Get

• Laminin Pentapeptide YIGSR-NH₂ (Highly Pure)
• Defined synthetic peptide for extracellular matrix-related research
• Suitable for cell adhesion, coating, and biomaterials workflows
• Useful in mechanistic and assay development studies
• For research use only (RUO)

Why Researchers Choose It

• Defined laminin-derived motif for controlled ECM-related experiments
• Useful in cell culture, biomaterials, and receptor interaction workflows
• Supports surface engineering and scaffold design studies
• Applicable to neural, epithelial, and tumor-related in vitro systems
• Compact peptide format enables flexible experimental design

Frequently Asked Questions (FAQ)

• What is YIGSR-NH₂ used for in research?
  It is commonly used in cell adhesion studies, extracellular matrix biology, biomaterials research, and cell culture workflows involving laminin-derived signaling or surface interactions.
• What does this peptide come from?
  YIGSR is a synthetic pentapeptide derived from the laminin B1 chain, a component of the extracellular matrix.
• Why is this peptide useful compared with full-length laminin?
  Short defined peptides can help researchers isolate specific biological interactions or signaling motifs without introducing the broader complexity of full-length extracellular matrix proteins.
• Can this peptide be used in coating or hydrogel applications?
  Yes, it is commonly relevant to workflows involving substrate coating, scaffold modification, hydrogel functionalization, and matrix-guided cell studies.
• Is this product intended for clinical or therapeutic use?
  No. This product is supplied strictly for research use only and is not intended for human or animal use, diagnostic procedures, or therapeutic applications.

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Safety

Users must review the Material Safety Data Sheet (MSDS) prior to handling. Avoid ingestion, inhalation, or contact with eyes, skin, or clothing.

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References

• Yin Y, Wang W, Shao Q, Li B, Yu D, Zhou X, Parajuli J, Xu H, Qiu T, Yetisen AK, Jiang N. Pentapeptide IKVAV-engineered hydrogels for neural stem cell attachment. Biomater Sci. 2021 Apr 21;9(8):2887-2892.
• Kim YY, Li H, Song YS, Jeong HS, Yun HY, Baek KJ, Kwon NS, Shin YK, Park KC, Kim DS. Laminin peptide YIGSR enhances epidermal development of skin equivalents. Am J Hosp Pharm. 1991 Mar;48(3):501-6.
• Graf J, Ogle RC, Robey FA, Sasaki M, Martin GR, Yamada Y, Kleinman HK. A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor. Biochemistry. 1987 Nov 3;26(22):6896-900.
• Jain R, Roy S. Tuning the gelation behavior of short laminin derived peptides via solvent mediated self-assembly. Mater Sci Eng C Mater Biol Appl. 2020 Mar;108:110483.
• Iwamoto Y, Robey FA, Graf J, Sasaki M, Kleinman HK, Yamada Y, Martin GR. YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science. 1987 Nov 20;238(4830):1132-4.
• Hadley MA, Weeks BS, Kleinman HK, Dym M. Laminin promotes formation of cord-like structures by Sertoli cells in vitro. Dev Biol. 1990 Aug;140(2):318-27.
• Dalet-Fumeron V, Boudjennah L, Pagano M. Binding of the cysteine proteinases papain and cathepsin B-like to coated laminin: use of synthetic peptides from laminin and from the laminin binding region of the beta 1 integrin subunit to characterize the binding site. Arch Biochem Biophys. 1998 Oct 15;358(2):283-90.
• Tung PS, Fritz IB. Interactions of Sertoli cells with laminin are essential to maintain integrity of the cytoskeleton and barrier functions of cells in culture in the two-chambered assembly. J Cell Physiol. 1993 Jul;156(1):1-11.
• Willette RN, Storer BL, Clark RK, Ohlstein EH. Human laminin produces human platelet aggregation in vitro. Life Sci. 1994;55(5):379-88.